Only in Titles

Search results for: Expression Systems

paperclip

Error loading info... Pleas try again later.
paperclip

#32619737   2020/06/30 To Up

Biosynthesis and tissue-specific partitioning of camphor and eugenol in Ocimum kilimandscharicum.

In Ocimum kilimandscharicum, the relative volatile composition of camphor in leaves was as high as 55%, while that of eugenol in roots was 57%. These metabolites were differentially partitioned between the aerial and root tissues. Global metabolomics revealed tissue-specific biochemical specialization, evident by the differential distribution of 2588 putative metabolites across nine tissues. Next-generation sequencing analysis indicated differential expression of 51 phenylpropanoid and 55 terpenoid pathway genes in aerial and root tissues. By integrating metabolomics with transcriptomics, the camphor biosynthesis pathway in O. kilimandscharicum was elucidated. In planta bioassays revealed the role of geranyl diphosphate synthase (gpps) and borneol dehydrogenase (bdh) in camphor biosynthesis. Further, the partitioning of camphor was attributed to tissue-specific gene expression of both the pathway entry point (gpps) and terminal (bdh) enzyme. Unlike camphor, eugenol accumulated more in roots; however, absence of the eugenol synthase gene in roots indicated long distance transport from aerial tissues. In silico co-expression analysis indicated the potential involvement of ATP-binding cassette, multidrug and toxic compound extrusion, and sugar transporters in eugenol transport. Similar partitioning was evident across five other Ocimum species. Overall, our work indicates that metabolite partitioning maybe a finely regulated process, which may have implications on plant growth, development, and defense.
Priyanka Singh, Raviraj M Kalunke, Anurag Shukla, Oren Tzfadia, Hirekodathakallu V Thulasiram, Ashok P Giri

2139 related Products with: Biosynthesis and tissue-specific partitioning of camphor and eugenol in Ocimum kilimandscharicum.

25 mg4 Membranes/Box

Related Pathways

paperclip

#32619572   2020/06/30 To Up

Analysis of chemosensory genes in Semiothisa cinerearia reveals sex-specific contributions for type-II sex pheromone chemosensation.

Insects employ a sensitive chemosensory system to accurately recognize external odorants, which help them to make a behavioral response quickly. Semiothisa cinerearia has caused serious damages to Sophora japonica L. in recent years, and there is still a lack of effective strategy to control the pest. Although the two type-II sex pheromones of S. cinerearia, 6Z,9Z-cis-3,4-epoxy-17:H and 3Z,6Z,9Z-17:H, have been identified for 30 years, the molecular mechanisms underlying the chemosensation of the two sex pheromones are still unknown. Here, we found that there are differences in the types of antennae sensilla between sexes, and revealed 146 putative chemosensory genes in the antennal transcriptome. Among these genes, 11 and 40 of them displayed male-biased and female-biased expression, respectively. Our findings greatly improve the chemosensory gene resources for S. cinerearia and provide a foundation for functional studies of these sex-biased genes on the chemosensation of sex pheromones and on other sex-related behaviors.
Xiu-Yun Zhu, Ji-Wei Xu, Lu-Lu Li, Dong-Yun Wang, Meng-Li Zhang, Nan-Nan Yu, Endang R Purba, Fan Zhang, Xiao-Ming Li, Ya-Nan Zhang, Ding-Ze Mang

1652 related Products with: Analysis of chemosensory genes in Semiothisa cinerearia reveals sex-specific contributions for type-II sex pheromone chemosensation.

0.1 ml0.2 mg0.1 mg25 µg250 ml100 TESTS0.2 mg1 ml1 LITRE25 µg0.1 mg100 ml

Related Pathways

paperclip

#32619498   2020/06/30 To Up

Translational quality control and reprogramming during stress adaptation.

Organisms encounter stress throughout their lives, and therefore require the ability to respond rapidly to environmental changes. Although transcriptional responses are crucial for controlling changes in gene expression, regulation at the translational level often allows for a faster response at the protein levels which permits immediate adaptation. The fidelity and robustness of protein synthesis are actively regulated under stress. For example, mistranslation can be beneficial to cells upon environmental changes and also alters cellular stress responses. Additionally, stress modulates both global and selective translational regulation through mechanisms including the change of aminoacyl-tRNA activity, tRNA pool reprogramming and ribosome heterogeneity. In this review, we draw on studies from both the prokaryotic and eukaryotic systems to discuss current findings of cellular adaptation at the level of translation, specifically translational fidelity and activity changes in response to a wide array of environmental stressors including oxidative stress, nutrient depletion, temperature variation, antibiotics and host colonization.
Nien-Ching Han, Paul Kelly, Michael Ibba

1232 related Products with: Translational quality control and reprogramming during stress adaptation.

5 x 1 ml100 Tests 0.1 mg 500

Related Pathways

paperclip

Error loading info... Pleas try again later.
paperclip

#32619469   // To Up

Pharmaceutical-Grade Rigosertib Is a Microtubule-Destabilizing Agent.

We recently used CRISPRi/a-based chemical-genetic screens and cell biological, biochemical, and structural assays to determine that rigosertib, an anti-cancer agent in phase III clinical trials, kills cancer cells by destabilizing microtubules. Reddy and co-workers (Baker et al., 2020, this issue of Molecular Cell) suggest that a contaminating degradation product in commercial formulations of rigosertib is responsible for the microtubule-destabilizing activity. Here, we demonstrate that cells treated with pharmaceutical-grade rigosertib (>99.9% purity) or commercially obtained rigosertib have qualitatively indistinguishable phenotypes across multiple assays. The two formulations have indistinguishable chemical-genetic interactions with genes that modulate microtubule stability, both destabilize microtubules in cells and in vitro, and expression of a rationally designed tubulin mutant with a mutation in the rigosertib binding site (L240F TUBB) allows cells to proliferate in the presence of either formulation. Importantly, the specificity of the L240F TUBB mutant for microtubule-destabilizing agents has been confirmed independently. Thus, rigosertib kills cancer cells by destabilizing microtubules, in agreement with our original findings.
Marco Jost, Yuwen Chen, Luke A Gilbert, Max A Horlbeck, Lenno Krenning, Grégory Menchon, Ankit Rai, Min Y Cho, Jacob J Stern, Andrea E Prota, Martin Kampmann, Anna Akhmanova, Michel O Steinmetz, Marvin E Tanenbaum, Jonathan S Weissman

1474 related Products with: Pharmaceutical-Grade Rigosertib Is a Microtubule-Destabilizing Agent.

100ug Lyophilized100ug Lyophilized100 ul1 mg100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

Related Pathways

paperclip

#32619289   2020/07/03 To Up

Transcriptional profiling of Pseudomonas aeruginosa PAO1 in response to anti-biofilm and anti-infection agent exopolysaccharide EPS273.

Relative few anti-biofilm polysaccharides against Pseudomonas aeruginosa were done to investigate the underlying molecular mechanism. Exopolysaccharide EPS273 can clearly reduce biofilm formation and infection of P. aeruginosa. This study aims to investigate its anti-biofilm and anti-infection mechanism on transcriptional level.
Zuodong Wu, Rikuan Zheng, Jing Zhang, Shimei Wu

1025 related Products with: Transcriptional profiling of Pseudomonas aeruginosa PAO1 in response to anti-biofilm and anti-infection agent exopolysaccharide EPS273.

0.1ml0.1ml0.1ml100 μg 100 UG100 100ug0.1 mg

Related Pathways

paperclip

#32619075   2020/07/03 To Up

The role of CAPG in molecular communication between the embryo and the uterine endometrium: Is its function conserved in species with different implantation strategies?

During the preimplantation period of pregnancy in eutherian mammals, transcriptional and proteomic changes in the uterine endometrium are required to facilitate receptivity to an implanting blastocyst. These changes are mediated, in part, by proteins produced by the developing conceptus (inner cell mass and extraembryonic membranes). We hypothesized that this common process in early pregnancy in eutheria may be facilitated by highly conserved conceptus-derived proteins such as macrophage capping protein (CAPG). We propose that CAPG may share functionality in modifying the transcriptome of the endometrial epithelial cells to facilitate receptivity to implantation in species with different implantation strategies. A recombinant bovine form of CAPG (91% sequence identity between bovine and human) was produced and bovine endometrial epithelial (bEECs) and stromal (bESCs) and human endometrial epithelial cells (hEECs) were cultured for 24 hours with and without recombinant bovine CAPG (rbCAPG). RNA sequencing and quantitative real-time PCR analysis were used to assess the transcriptional response to rbCAPG (Control, vehicle, CAPG 10, 100, 1000 ng/mL: n = 3 biological replicates per treatment per species). Treatment of bEECs with CAPG resulted in alterations in the abundance of 1052 transcripts (629 increased and 423 decreased) compared to vehicle controls. Treatment of hEECs with bovine CAPG increased expression of transcripts previously known to interact with CAPG in different systems (CAPZB, CAPZA2, ADD1, and ADK) compared with vehicle controls (P < .05). In conclusion, we have demonstrated that CAPG, a highly conserved protein in eutherian mammals, elicits a transcriptional response in the endometrial epithelium in species with different implantation strategies that may contribute to pregnancy success.
Haidee Tinning, Alysha Taylor, Dapeng Wang, Bede Constantinides, Ruth Sutton, Georgios Oikonomou, Miguel A Velazquez, Paul Thompson, Achim Treumann, Mary J O'Connell, Niamh Forde

1115 related Products with: The role of CAPG in molecular communication between the embryo and the uterine endometrium: Is its function conserved in species with different implantation strategies?

1 100ul 100ul96T

Related Pathways

paperclip

#32618081   2020/07/02 To Up

CRISPR/Cas9-mediated whole genomic wide knockout screening identifies mitochondrial ribosomal proteins involving in oxygen-glucose deprivation/reperfusion resistance.

Recanalization therapy by intravenous thrombolysis or endovascular therapy is critical for the treatment of cerebral infarction. However, the recanalization treatment will also exacerbate acute brain injury and even severely threatens human life due to the reperfusion injury. So far, the underlying mechanisms for cerebral ischaemia-reperfusion injury are poorly understood and effective therapeutic interventions are yet to be discovered. Therefore, in the research, we subjected SK-N-BE(2) cells to oxygen-glucose deprivation/reperfusion (OGDR) insult and performed a pooled genome-wide CRISPR (clustered regularly interspaced short palindromic repeats)/Cas9 (CRISPR-associated protein 9) knockout screen to discover new potential therapeutic targets for cerebral ischaemia-reperfusion injury. We used Metascape to identify candidate genes which might involve in OGDR resistance. We found that the genes contributed to OGDR resistance were primarily involved in neutrophil degranulation, mitochondrial translation, and regulation of cysteine-type endopeptidase activity involved in apoptotic process and response to oxidative stress. We then knocked down some of the identified candidate genes individually. We demonstrated that MRPL19, MRPL32, MRPL52 and MRPL51 inhibition increased cell viability and attenuated OGDR-induced apoptosis. We also demonstrated that OGDR down-regulated the expression of MRPL19 and MRPL51 protein. Taken together, our data suggest that genome-scale screening with Cas9 is a reliable tool to analyse the cellular systems that respond to OGDR injury. MRPL19 and MRPL51 contribute to OGDR resistance and are supposed to be promising targets for the treatment of cerebral ischaemia-reperfusion damage.
Xinjie Guan, Hainan Zhang, Haiyun Qin, Chunli Chen, Zhiping Hu, Jieqiong Tan, Liuwang Zeng

1009 related Products with: CRISPR/Cas9-mediated whole genomic wide knockout screening identifies mitochondrial ribosomal proteins involving in oxygen-glucose deprivation/reperfusion resistance.

100100 assays1 mg100 assays1mg50 2 Pieces/Box5001mg2050

Related Pathways

paperclip

#32617841   2020/07/02 To Up

Construction of an Efficient Nicotinate Dehydrogenase Expression System in Comamonas testosteroni CNB-2 with Multi-level N-Terminal Engineering.

Nicotinate dehydrogenase (NDHase) is a membrane protein with three subunits (ndhS, ndhL, and ndhM), which is difficult to express in a functional form using common hosts such as Escherichia coli, Bacillus subtilis, or Pichia pastoris. Comamonas testosteroni is a suitable microbial chassis for expressing multi-subunit membrane proteins. However, the expression of NDHase in C. testosteroni is extremely low. We have developed a systematic approach to create an efficient protein expression system in C. testosteroni CNB-2 using multi-level N-terminal engineering. We selected a strong promoter for the Mmp1 system that enables control of transcriptional strength in unconventional bacteria. This enhanced the expression of a green fluorescent reporter protein threefold. Following modification of the N-terminal Shine-Dalgarno sequence and rearrangement of amino acid sequence in the starting area of the gene encoding NDHase, enzyme activity increased from 90.6 to 165 U/L. These optimized N-terminal Shine-Dalgarno and amino acid sequences were used to enhance the expression of ndhL subunit and improve the balance expression of three subunits of NDHase, resulting in enzyme activity of 192 U/L that far surpasses the previously reported level. These results highlight a promising strategy for the development of other heterologous expression systems for challenging proteins using unconventional bacteria.
Zhen-Hua Lu, Li-Rong Yang, Jian-Ping Wu

1946 related Products with: Construction of an Efficient Nicotinate Dehydrogenase Expression System in Comamonas testosteroni CNB-2 with Multi-level N-Terminal Engineering.

200ul100 μg250ul200ul25mg200ul100ug Lyophilized250ul200ul250ul200ul100ug Lyophilized

Related Pathways